ID   G6PD4_ARATH             Reviewed;         625 AA.
AC   Q93ZW0; O80525;
DT   25-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2001, sequence version 1.
DT   24-JAN-2024, entry version 155.
DE   RecName: Full=Inactive glucose-6-phosphate 1-dehydrogenase 4, chloroplastic {ECO:0000305};
DE            Short=AtG6PD4 {ECO:0000303|PubMed:15634201};
DE            Short=G6PDH4 {ECO:0000305};
DE   Flags: Precursor;
GN   Name=G6PD4 {ECO:0000303|PubMed:15634201};
GN   OrderedLocusNames=At1g09420 {ECO:0000312|Araport:AT1G09420};
GN   ORFNames=F14J9.8 {ECO:0000312|EMBL:AAC33202.1};
OS   Arabidopsis thaliana (Mouse-ear cress).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX   NCBI_TaxID=3702;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=11130712; DOI=10.1038/35048500;
RA   Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA   Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA   Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA   Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA   Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA   Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA   Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA   Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA   Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA   Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA   Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA   Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA   Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA   Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA   Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT   "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL   Nature 408:816-820(2000).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Columbia;
RX   PubMed=27862469; DOI=10.1111/tpj.13415;
RA   Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA   Town C.D.;
RT   "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT   genome.";
RL   Plant J. 89:789-804(2017).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=14593172; DOI=10.1126/science.1088305;
RA   Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA   Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA   Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA   Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA   Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA   Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA   Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA   Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA   Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA   Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA   Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA   Ecker J.R.;
RT   "Empirical analysis of transcriptional activity in the Arabidopsis
RT   genome.";
RL   Science 302:842-846(2003).
RN   [4]
RP   TISSUE SPECIFICITY.
RX   PubMed=15634201; DOI=10.1111/j.1365-313x.2004.02293.x;
RA   Wakao S., Benning C.;
RT   "Genome-wide analysis of glucose-6-phosphate dehydrogenases in
RT   Arabidopsis.";
RL   Plant J. 41:243-256(2005).
RN   [5]
RP   FUNCTION, INTERACTION WITH G6PD1, SUBCELLULAR LOCATION, AND MUTAGENESIS OF
RP   CYS-212 AND CYS-220.
RX   PubMed=21309870; DOI=10.1111/j.1365-313x.2011.04535.x;
RA   Meyer T., Hoelscher C., Schwoeppe C., von Schaewen A.;
RT   "Alternative targeting of Arabidopsis plastidic glucose-6-phosphate
RT   dehydrogenase G6PD1 involves cysteine-dependent interaction with G6PD4 in
RT   the cytosol.";
RL   Plant J. 66:745-758(2011).
CC   -!- FUNCTION: Seems to be a catalytically inactive enzyme.
CC       {ECO:0000269|PubMed:21309870}.
CC   -!- SUBUNIT: Forms homodimer (By similarity). Interacts with G6PD1
CC       (PubMed:21309870). {ECO:0000250|UniProtKB:P11411,
CC       ECO:0000269|PubMed:21309870}.
CC   -!- SUBCELLULAR LOCATION: Plastid, chloroplast stroma
CC       {ECO:0000269|PubMed:21309870}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=1;
CC         Comment=A number of isoforms are produced. According to EST
CC         sequences. {ECO:0000305};
CC       Name=1;
CC         IsoId=Q93ZW0-1; Sequence=Displayed;
CC   -!- TISSUE SPECIFICITY: Expressed in leaves, stems and buds.
CC       {ECO:0000269|PubMed:15634201}.
CC   -!- MISCELLANEOUS: There are 6 glucose-6-phosphate 1-dehydrogenase genes in
CC       A.thaliana. {ECO:0000303|PubMed:15634201}.
CC   -!- SIMILARITY: Belongs to the glucose-6-phosphate dehydrogenase family.
CC       {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAC33202.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; AC003970; AAC33202.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; CP002684; AEE28440.1; -; Genomic_DNA.
DR   EMBL; AY056232; AAL07081.1; -; mRNA.
DR   EMBL; AY117271; AAM51346.1; -; mRNA.
DR   PIR; E86227; E86227.
DR   RefSeq; NP_563844.1; NM_100813.2. [Q93ZW0-1]
DR   AlphaFoldDB; Q93ZW0; -.
DR   SMR; Q93ZW0; -.
DR   BioGRID; 22706; 2.
DR   STRING; 3702.Q93ZW0; -.
DR   PaxDb; 3702-AT1G09420-2; -.
DR   ProteomicsDB; 230469; -. [Q93ZW0-1]
DR   EnsemblPlants; AT1G09420.1; AT1G09420.1; AT1G09420. [Q93ZW0-1]
DR   GeneID; 837465; -.
DR   Gramene; AT1G09420.1; AT1G09420.1; AT1G09420. [Q93ZW0-1]
DR   KEGG; ath:AT1G09420; -.
DR   Araport; AT1G09420; -.
DR   TAIR; AT1G09420; G6PD4.
DR   eggNOG; KOG0563; Eukaryota.
DR   HOGENOM; CLU_013524_1_0_1; -.
DR   InParanoid; Q93ZW0; -.
DR   PhylomeDB; Q93ZW0; -.
DR   BioCyc; ARA:AT1G09420-MONOMER; -.
DR   BRENDA; 1.1.1.49; 399.
DR   PRO; PR:Q93ZW0; -.
DR   Proteomes; UP000006548; Chromosome 1.
DR   ExpressionAtlas; Q93ZW0; baseline and differential.
DR   GO; GO:0009570; C:chloroplast stroma; IEA:UniProtKB-SubCell.
DR   GO; GO:0004345; F:glucose-6-phosphate dehydrogenase activity; IEA:InterPro.
DR   GO; GO:0050661; F:NADP binding; IEA:InterPro.
DR   GO; GO:0006006; P:glucose metabolic process; IEA:UniProtKB-KW.
DR   GO; GO:0006098; P:pentose-phosphate shunt; IEA:UniProt.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR   HAMAP; MF_00966; G6PD; 1.
DR   InterPro; IPR001282; G6P_DH.
DR   InterPro; IPR022675; G6P_DH_C.
DR   InterPro; IPR022674; G6P_DH_NAD-bd.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   NCBIfam; TIGR00871; zwf; 1.
DR   PANTHER; PTHR23429; GLUCOSE-6-PHOSPHATE 1-DEHYDROGENASE G6PD; 1.
DR   PANTHER; PTHR23429:SF4; INACTIVE GLUCOSE-6-PHOSPHATE 1-DEHYDROGENASE 4, CHLOROPLASTIC; 1.
DR   Pfam; PF02781; G6PD_C; 1.
DR   Pfam; PF00479; G6PD_N; 1.
DR   PRINTS; PR00079; G6PDHDRGNASE.
DR   SUPFAM; SSF55347; Glyceraldehyde-3-phosphate dehydrogenase-like, C-terminal domain; 1.
DR   SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR   Genevisible; Q93ZW0; AT.
PE   1: Evidence at protein level;
KW   Alternative splicing; Carbohydrate metabolism; Chloroplast; Disulfide bond;
KW   Glucose metabolism; NADP; Plastid; Reference proteome; Transit peptide.
FT   TRANSIT         1..49
FT                   /note="Chloroplast"
FT                   /evidence="ECO:0000255"
FT   CHAIN           50..625
FT                   /note="Inactive glucose-6-phosphate 1-dehydrogenase 4,
FT                   chloroplastic"
FT                   /id="PRO_0000010438"
FT   BINDING         160..167
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250|UniProtKB:P11413"
FT   BINDING         194
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250|UniProtKB:P11413"
FT   BINDING         297
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250|UniProtKB:P11413"
FT   DISULFID        212..220
FT                   /note="Redox modulation"
FT                   /evidence="ECO:0000250|UniProtKB:Q43839"
FT   MUTAGEN         212
FT                   /note="C->S: Abolishes interaction with G6PD1."
FT                   /evidence="ECO:0000269|PubMed:21309870"
FT   MUTAGEN         220
FT                   /note="C->S: Abolishes interaction with G6PD1."
FT                   /evidence="ECO:0000269|PubMed:21309870"
SQ   SEQUENCE   625 AA;  70202 MW;  83D9F8D96F0B66F4 CRC64;
     MSLSSCLLPF SQSATAPSSS VCSCHLAASF SNFPVSSRDY SFSRSGSLVL NGGGSNLCRR
     FCGLKLWILK SLNRRQGNNR KHQPVNELTT HSKHTFLSDD ERGFAEETRA EDLRPEENIL
     GTDLNDGFHN VGDLPPVSKQ LSDDLSDVRR RASLCIAVVG ATGELARGKI FPALFALYYS
     GYLPEDVAIF GVSRKNLTDE DLRSIIASTL TCRVDHQENC GGKMDAFQSR TYYINGGYNN
     RDGMSRLAER MKQIEGESEA NRIFYLSVPQ EALVDVACTI GDNAQAPRGW TRIIVEKPFG
     FNSHSSHQLT KSLLSKFEEK QIYRIDHMLG RNLIENLTVL RFSNLVFEPL WNRTYIRNIQ
     VIISESIAQT EKFSDGYGII RDIVHSHILQ TIALLAMEPP ISLDGEDIRN EKVKVLRSIR
     KIDPRDVILG QYKSSSRDKN GVILNGVDPT YCAAALYIDN ARWDGVPFLV RVGTGLIKHR
     VEIHVQFRHV PGNLYRENIG INIDLGTNEL ILRDEPDEAI LVKINNKVPG LGLQLDASEL
     NLLYKDRYKT EVPDSYEHLI HDVIDGDNHL FMRSDEVAAA WNILSPVLEE IDKHHTAPEL
     YEFGGRGPVA AYYLWAKHGV PWADD
//